ArticleThe Journal of biological chemistry2015
Miropin, a novel bacterial serpin from the periodontopathogen Tannerella forsythia, inhibits a broad range of proteases by using different peptide bonds within the reactive center loop.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 48 citations in OpenAlex.
- Interspecies regulation of virulence through gingipain inhibition by a Tannerella forsythia serpin.EMBO reports · 2026Article
- Periodontal pathogens and cancer development.Periodontology 2000 · 2024Review
- Recent Aspects of Periodontitis and Alzheimer's Disease-A Narrative Review.International journal of molecular sciences · 2024Review
- The intriguing strategies ofFrontiers in oral health · 2024Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- DNA accelerates the protease inhibition of a bacterial serpin chloropin.Frontiers in molecular biosciences · 2023Article
- Ecotin: A versatile protease inhibitor of bacteria and eukaryotes.Frontiers in microbiology · 2023Review
- Article
- Serpins in Tick Physiology and Tick-Host Interaction.Frontiers in cellular and infection microbiology · 2022Review
- The Serpin Superfamily and Their Role in the Regulation and Dysfunction of Serine Protease Activity in COPD and Other Chronic Lung Diseases.International journal of molecular sciences · 2021Review
- Gut Serpinome: Emerging Evidence in IBD.International journal of molecular sciences · 2021Review
- Periodontal Pathogens' strategies disarm neutrophils to promote dysregulated inflammation.Molecular oral microbiology · 2021Review
- Digestive Inflammation: Role of Proteolytic Dysregulation.International journal of molecular sciences · 2021Review
- Periodontitis Exacerbates and Promotes the Progression of Chronic Kidney Disease Through Oral Flora, Cytokines, and Oxidative Stress.Frontiers in microbiology · 2021Review
- Uncovering the Oral Dysbiotic Microbiota as Masters of Neutrophil Responses in the Pathobiology of Periodontitis.Frontiers in microbiology · 2021Review
- Interactions Between Neutrophils and Periodontal Pathogens in Late-Onset Periodontitis.Frontiers in cellular and infection microbiology · 2021Review
- Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia.BMC genomics · 2020Article
- Plasmin inhibition by bacterial serpin: Implications in gum disease.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- The role ofInfectious agents and cancer · 2019Review
- Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
All prokaryotic genes encoding putative serpins identified to date are found in environmental and commensal microorganisms, and only very few prokaryotic serpins have been investigated from a mechanistic standpoint. Herein, we characterized a novel serpin (miropin) from the human pathogen Tannerella forsythia, a bacterium implicated in initiation and progression of human periodontitis. In contrast to other serpins, miropin efficiently inhibited a broad range of proteases (neutrophil and pancreatic elastases, cathepsin G, subtilisin, and trypsin) with a stoichiometry of inhibition of around 3 and second-order association rate constants that ranged from 2.7 × 10(4) (cathepsin G) to 7.1 × 10(5) m(-1)s(-1) (subtilisin). Inhibition was associated with the formation of complexes that were stable during SDS-PAGE. The unusually broad specificity of miropin for target proteases is achieved through different active sites within the reactive center loop upstream of the P1-P1' site, which was predicted from an alignment of the primary structure of miropin with those of well studied human and prokaryotic serpins. Thus, miropin is unique among inhibitory serpins, and it has apparently evolved the ability to inhibit a multitude of proteases at the expense of a high stoichiometry of inhibition and a low association rate constant. These characteristics suggest that miropin arose as an adaptation to the highly proteolytic environment of subgingival plaque, which is exposed continually to an array of host proteases in the inflammatory exudate. In such an environment, miropin may function as an important virulence factor by protecting bacterium from the destructive activity of neutrophil serine proteases. Alternatively, it may act as a housekeeping protein that regulates the activity of endogenous T. forsythia serine proteases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.